ID GSTUK_ARATH Reviewed; 217 AA. AC Q8L7C9; Q8LBS3; Q9M9F4; DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 24-JAN-2024, entry version 144. DE RecName: Full=Glutathione S-transferase U20 {ECO:0000303|PubMed:12090627}; DE Short=AtGSTU20 {ECO:0000303|PubMed:12090627}; DE EC=2.5.1.18 {ECO:0000269|PubMed:17220357, ECO:0000269|PubMed:28223489}; DE AltName: Full=FIN219-interacting protein 1 {ECO:0000303|PubMed:17220357}; DE AltName: Full=GST class-tau member 20 {ECO:0000303|PubMed:12090627}; GN Name=GSTU20 {ECO:0000303|PubMed:12090627}; GN Synonyms=FIP1 {ECO:0000303|PubMed:17220357}; GN OrderedLocusNames=At1g78370 {ECO:0000312|Araport:AT1G78370}; GN ORFNames=F3F9.11 {ECO:0000312|EMBL:AAF71798.1}; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Columbia; RX PubMed=11130712; DOI=10.1038/35048500; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., RA Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."; RL Nature 408:816-820(2000). RN [2] RP GENOME REANNOTATION. RC STRAIN=cv. Columbia; RX PubMed=27862469; DOI=10.1111/tpj.13415; RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S., RA Town C.D.; RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference RT genome."; RL Plant J. 89:789-804(2017). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=cv. Columbia; RX PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L., RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., RA Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., RA Feldmann K.A.; RT "Full-length cDNA from Arabidopsis thaliana."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP GENE FAMILY, AND NOMENCLATURE. RX PubMed=12090627; DOI=10.1023/a:1015557300450; RA Wagner U., Edwards R., Dixon D.P., Mauch F.; RT "Probing the diversity of the Arabidopsis glutathione S-transferase gene RT family."; RL Plant Mol. Biol. 49:515-532(2002). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16829588; DOI=10.1104/pp.106.079509; RA Foley R.C., Sappl P.G., Perl-Treves R., Millar A.H., Singh K.B.; RT "Desensitization of GSTF8 induction by a prior chemical treatment is long RT lasting and operates in a tissue-dependent manner."; RL Plant Physiol. 142:245-253(2006). RN [7] RP FUNCTION, INTERACTION WITH JAR1/FIN219, DISRUPTION PHENOTYPE, TISSUE RP SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL RP PROPERTIES, AND CATALYTIC ACTIVITY. RC STRAIN=cv. Columbia; RX PubMed=17220357; DOI=10.1104/pp.106.094185; RA Chen I.-C., Huang I.-C., Liu M.-J., Wang Z.-G., Chung S.-S., Hsieh H.-L.; RT "Glutathione S-transferase interacting with far-red insensitive 219 is RT involved in phytochrome A-mediated signaling in Arabidopsis."; RL Plant Physiol. 143:1189-1202(2007). RN [8] RP FUNCTION, AND INDUCTION BY GRAVITY. RC STRAIN=cv. Columbia; TISSUE=Flower; RX PubMed=23281391; DOI=10.3732/ajb.1200339; RA Schenck C.A., Nadella V., Clay S.L., Lindner J., Abrams Z., Wyatt S.E.; RT "A proteomics approach identifies novel proteins involved in gravitropic RT signal transduction."; RL Am. J. Bot. 100:194-202(2013). RN [9] RP X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) IN COMPLEX WITH JAR1/FIN219 AND RP GLUTATHIONE, FUNCTION, HOMODIMER, CATALYTIC ACTIVITY, AND ACTIVITY RP REGULATION. RX PubMed=28223489; DOI=10.1073/pnas.1609980114; RA Chen C.-Y., Ho S.-S., Kuo T.-Y., Hsieh H.-L., Cheng Y.-S.; RT "Structural basis of jasmonate-amido synthetase FIN219 in complex with RT glutathione S-transferase FIP1 during the JA signal regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 114:E1815-E1824(2017). CC -!- FUNCTION: Exhibits glutathione-dependent thiol transferase activities. CC Can use glutathione (GSH) and 1-chloro-2,4-dinitrobenzene (CDNB) as CC substrates. Involved in the regulation of far-red light influence on CC development (PubMed:17220357). Regulator of the interplay between light CC and JA signaling by increasing JAR1/FIN219 efficiency CC (PubMed:28223489). Maybe involved in gravitropic signal transduction CC (Probable). {ECO:0000269|PubMed:17220357, ECO:0000269|PubMed:28223489, CC ECO:0000305|PubMed:23281391}. CC -!- CATALYTIC ACTIVITY: CC Reaction=glutathione + RX = a halide anion + an S-substituted CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, CC ChEBI:CHEBI:90779; EC=2.5.1.18; CC Evidence={ECO:0000269|PubMed:17220357, ECO:0000269|PubMed:28223489}; CC -!- ACTIVITY REGULATION: Activated by JAR1/FIN219. CC {ECO:0000269|PubMed:28223489}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.467 mM for glutathione {ECO:0000269|PubMed:17220357}; CC KM=1.794 mM for 1-chloro-2,4- dinitrobenzene CC {ECO:0000269|PubMed:17220357}; CC -!- SUBUNIT: Homodimerization. Interacts with JAR1/FIN219 under continuous CC far red (cFR) light to stimulate JAR1/FIN219 activity and substrate CC selectivity. {ECO:0000269|PubMed:17220357, CC ECO:0000269|PubMed:28223489}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17220357}. Cytoplasm, CC cytosol {ECO:0000269|PubMed:17220357}. CC -!- TISSUE SPECIFICITY: Mostly associated with vascular tissues, especially CC near hydathodes. {ECO:0000269|PubMed:17220357}. CC -!- DEVELOPMENTAL STAGE: Light-dependent expression. Developmentally CC regulated. First observed in cotyledon vascular tissues of young CC seedlings. Appears at the shoot apex, in the upper part of hypocotyls CC and in roots in one week old seedlings. Later highly expressed in the CC basal portion of trichomes, veins, shoot apex, and hypocotyls. Becomes CC restricted to the margins of leaves and in roots. In drakness and blue CC light (B) grown plants, localized in cotyledons vascular tissues. In CC far-red (FR) and red (R) light conditions, mostly confined to regions CC of vascular tissues near the hydathode of cotyledons. In adult plants, CC expressed in vascular tissues of flower organs. CC {ECO:0000269|PubMed:17220357}. CC -!- INDUCTION: Induced by a gravistimulation. CC {ECO:0000269|PubMed:23281391}. CC -!- DISRUPTION PHENOTYPE: Hyposensitive hypocotyl phenotype under CC continuous far red (cFR) light and a delayed flowering phenotype under CC long-day conditions. {ECO:0000269|PubMed:17220357}. CC -!- SIMILARITY: Belongs to the GST superfamily. Tau family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF71798.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC013430; AAF71798.1; ALT_SEQ; Genomic_DNA. DR EMBL; CP002684; AEE36098.1; -; Genomic_DNA. DR EMBL; AY136338; AAM97004.1; -; mRNA. DR EMBL; BT000168; AAN15487.1; -; mRNA. DR EMBL; AY087026; AAM64587.1; -; mRNA. DR RefSeq; NP_177958.1; NM_106484.4. DR PDB; 5ECH; X-ray; 2.14 A; B/C/E/F=1-217. DR PDB; 5ECI; X-ray; 1.56 A; B/C/E/F=1-217. DR PDB; 5ECK; X-ray; 1.54 A; B/C/E/F=1-217. DR PDB; 5ECL; X-ray; 1.85 A; B/C/E/F=1-217. DR PDB; 5ECM; X-ray; 1.60 A; B/C/E/F=1-217. DR PDB; 5ECN; X-ray; 1.72 A; B/C/E/F=1-217. DR PDB; 5ECO; X-ray; 1.80 A; B/C/E/F=1-217. DR PDB; 5ECP; X-ray; 2.25 A; B/C/E/F=1-217. DR PDB; 5ECQ; X-ray; 1.66 A; B/C/E/F=1-217. DR PDB; 5ECR; X-ray; 1.72 A; B/C/E/F=1-217. DR PDB; 5ECS; X-ray; 1.65 A; A/B=1-217. DR PDBsum; 5ECH; -. DR PDBsum; 5ECI; -. DR PDBsum; 5ECK; -. DR PDBsum; 5ECL; -. DR PDBsum; 5ECM; -. DR PDBsum; 5ECN; -. DR PDBsum; 5ECO; -. DR PDBsum; 5ECP; -. DR PDBsum; 5ECQ; -. DR PDBsum; 5ECR; -. DR PDBsum; 5ECS; -. DR AlphaFoldDB; Q8L7C9; -. DR SMR; Q8L7C9; -. DR BioGRID; 29392; 4. DR STRING; 3702.Q8L7C9; -. DR iPTMnet; Q8L7C9; -. DR PaxDb; 3702-AT1G78370-1; -. DR ProteomicsDB; 247262; -. DR EnsemblPlants; AT1G78370.1; AT1G78370.1; AT1G78370. DR GeneID; 844173; -. DR Gramene; AT1G78370.1; AT1G78370.1; AT1G78370. DR KEGG; ath:AT1G78370; -. DR Araport; AT1G78370; -. DR TAIR; AT1G78370; GSTU20. DR eggNOG; KOG0406; Eukaryota. DR HOGENOM; CLU_011226_18_2_1; -. DR InParanoid; Q8L7C9; -. DR OMA; FESREED; -. DR OrthoDB; 767442at2759; -. DR PhylomeDB; Q8L7C9; -. DR BioCyc; ARA:AT1G78370-MONOMER; -. DR SABIO-RK; Q8L7C9; -. DR PRO; PR:Q8L7C9; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; Q8L7C9; baseline and differential. DR GO; GO:0048046; C:apoplast; HDA:TAIR. DR GO; GO:0009507; C:chloroplast; HDA:TAIR. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:TAIR. DR GO; GO:0005739; C:mitochondrion; HDA:TAIR. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0043295; F:glutathione binding; IDA:UniProtKB. DR GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB. DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro. DR GO; GO:2000030; P:regulation of response to red or far red light; IMP:UniProtKB. DR GO; GO:0009629; P:response to gravity; IEP:UniProtKB. DR GO; GO:0009407; P:toxin catabolic process; TAS:TAIR. DR CDD; cd03185; GST_C_Tau; 1. DR CDD; cd03058; GST_N_Tau; 1. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. DR InterPro; IPR010987; Glutathione-S-Trfase_C-like. DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf. DR InterPro; IPR040079; Glutathione_S-Trfase. DR InterPro; IPR004045; Glutathione_S-Trfase_N. DR InterPro; IPR045074; GST_C_Tau. DR InterPro; IPR045073; Omega/Tau-like. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR11260:SF601; GLUTATHIONE S-TRANSFERASE U20; 1. DR PANTHER; PTHR11260; GLUTATHIONE S-TRANSFERASE, GST, SUPERFAMILY, GST DOMAIN CONTAINING; 1. DR Pfam; PF13410; GST_C_2; 1. DR Pfam; PF02798; GST_N; 1. DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1. DR SFLD; SFLDG01152; Main.3:_Omega-_and_Tau-like; 1. DR SUPFAM; SSF47616; GST C-terminal domain-like; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS50405; GST_CTER; 1. DR PROSITE; PS50404; GST_NTER; 1. DR Genevisible; Q8L7C9; AT. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Detoxification; Growth regulation; Nucleus; KW Reference proteome; Transferase. FT CHAIN 1..217 FT /note="Glutathione S-transferase U20" FT /id="PRO_0000403932" FT DOMAIN 3..82 FT /note="GST N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00684" FT DOMAIN 88..208 FT /note="GST C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00685" FT BINDING 13 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000269|PubMed:28223489, FT ECO:0007744|PDB:5ECH, ECO:0007744|PDB:5ECI, FT ECO:0007744|PDB:5ECK, ECO:0007744|PDB:5ECL, FT ECO:0007744|PDB:5ECM, ECO:0007744|PDB:5ECN, FT ECO:0007744|PDB:5ECO, ECO:0007744|PDB:5ECP, FT ECO:0007744|PDB:5ECQ, ECO:0007744|PDB:5ECR, FT ECO:0007744|PDB:5ECS" FT BINDING 54 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000269|PubMed:28223489, FT ECO:0007744|PDB:5ECH, ECO:0007744|PDB:5ECI, FT ECO:0007744|PDB:5ECK, ECO:0007744|PDB:5ECL, FT ECO:0007744|PDB:5ECM, ECO:0007744|PDB:5ECN, FT ECO:0007744|PDB:5ECO, ECO:0007744|PDB:5ECP, FT ECO:0007744|PDB:5ECQ, ECO:0007744|PDB:5ECR, FT ECO:0007744|PDB:5ECS" FT BINDING 67 FT /ligand="glutathione" FT /ligand_id="ChEBI:CHEBI:57925" FT /evidence="ECO:0000269|PubMed:28223489, FT ECO:0007744|PDB:5ECH, ECO:0007744|PDB:5ECI, FT ECO:0007744|PDB:5ECK, ECO:0007744|PDB:5ECL, FT ECO:0007744|PDB:5ECM, ECO:0007744|PDB:5ECN, FT ECO:0007744|PDB:5ECO, ECO:0007744|PDB:5ECP, FT ECO:0007744|PDB:5ECQ, ECO:0007744|PDB:5ECR, FT ECO:0007744|PDB:5ECS" FT CONFLICT 181 FT /note="K -> N (in Ref. 4; AAM64587)" FT /evidence="ECO:0000305" FT STRAND 6..9 FT /evidence="ECO:0007829|PDB:5ECK" FT HELIX 14..26 FT /evidence="ECO:0007829|PDB:5ECK" FT STRAND 31..34 FT /evidence="ECO:0007829|PDB:5ECK" FT HELIX 37..39 FT /evidence="ECO:0007829|PDB:5ECS" FT HELIX 42..47 FT /evidence="ECO:0007829|PDB:5ECK" FT TURN 49..51 FT /evidence="ECO:0007829|PDB:5ECK" FT STRAND 56..59 FT /evidence="ECO:0007829|PDB:5ECK" FT STRAND 62..66 FT /evidence="ECO:0007829|PDB:5ECK" FT HELIX 67..77 FT /evidence="ECO:0007829|PDB:5ECK" FT STRAND 80..82 FT /evidence="ECO:0007829|PDB:5ECR" FT HELIX 89..103 FT /evidence="ECO:0007829|PDB:5ECK" FT HELIX 105..115 FT /evidence="ECO:0007829|PDB:5ECK" FT HELIX 119..139 FT /evidence="ECO:0007829|PDB:5ECK" FT STRAND 143..150 FT /evidence="ECO:0007829|PDB:5ECK" FT HELIX 152..158 FT /evidence="ECO:0007829|PDB:5ECK" FT TURN 159..162 FT /evidence="ECO:0007829|PDB:5ECK" FT HELIX 164..170 FT /evidence="ECO:0007829|PDB:5ECK" FT HELIX 175..178 FT /evidence="ECO:0007829|PDB:5ECK" FT HELIX 180..189 FT /evidence="ECO:0007829|PDB:5ECK" FT TURN 193..198 FT /evidence="ECO:0007829|PDB:5ECK" FT HELIX 202..215 FT /evidence="ECO:0007829|PDB:5ECK" SQ SEQUENCE 217 AA; 25006 MW; 5BD5DEB175079DA9 CRC64; MANLPILLDY WPSMFGMRAR VALREKGVEF EYREEDFSNK SPLLLQSNPI HKKIPVLVHN GKPVCESLNV VQYVDEAWPE KNPFFPSDPY GRAQARFWAD FVDKKFTDAQ FKVWGKKGEE QEAGKKEFIE AVKILESELG DKPYFGGDSF GYVDISLITF SSWFQAYEKF GNFSIESESP KLIAWAKRCM EKESVSKSLP DSEKIVAYAA EYRKNNL //